Plus d’anticorps contre F2R partenaires d’interaction

The activation of PAR-1 on the cell surface of SGC7901 and AGS cells was significantly reduced after the knockdown of EPCR. By contrast, blockade of PAR-1 reduced the proliferation and migration of gastric cells in vitro

Our structural data showed subtle changes in the binding pose between Vorapaxar and F16357. Transmembrane helices 1, 2, 5, and 7 were most significantly affected; most notably a large kink at F279(5.47) in TM helix 5 of the Vorapaxar complex was completely absent in the F16357 complex. The results of this study facilitate the future development of other therapeutic PAR1 antagonists.

Platelets were activated in antineutrophil cytoplasmic antibody (ANCA)-associated vasculitis (AAV) patients, and such activation was at least partially attributed to the thrombin-protease-activated receptors (PARs) pathway.

Study demonstrated that nerve activation by mucosal biopsy supernatants depends on proteases. This is a common feature of quiescent ulcerative colitis and irritable bowel syndrome (IBS) and may relate to some common gastrointestinal symptoms. However, only proteases in IBS supernatants signal through PAR1.

we found that activation of the protease-activated receptor 1 (PAR1) induced secretion of TSLP by the corneal stromal cells... we proposed that TSLP might function as the link between increased protease activity and inflammatory responses or itch sensation in the

In this study, we found upregulation of several hemostasis-related genes, including the thrombin-activatable receptor PAR-1 (protease-activated receptor-1), in Runx1/Cbfb-deleted MLL-AF9 cells. Similar to the effect of Runx1/Cbfb deletion, PAR-1 overexpression induced CDKN1A/p21 expression and attenuated proliferation in MLL-AF9 cells

Data highlight functional differences in proliferation and barrier integrity between dark keratinocytes and fair keratinocytes that are partly associated with their differential expression of PAR1 and PAR2.

the contribution of PAR1 and PAR4 to thrombin-mediated activation of the platelet fibrin receptor (GPIIbIIIa), is reported.

PAR1 in its inactive unligated state functions as a scaffold for TGFbetaRII to downregulate TGF-beta signaling, and thereby promote embryonic stem cell transition to functional endothelial cells.

this study shows that poly I:C treated PAR-1-/- mice given the thrombin inhibitor dabigatran etexilate exhibited less IFNbeta and CXCL10 expression in the spleen and plasma

Brain water content in the ipsilateral hemisphere and the tumor mass were significantly lower in PAR-1 KO than WT mice at day 12 after implantation of glioma cells.

The results of this study suggested that polarized microglia occur dynamically after ICH and that PAR-1 plays a role in the microglia activation and polarization.

In this study, we found upregulation of several hemostasis-related genes, including the thrombin-activatable receptor PAR-1 (protease-activated receptor-1), in Runx1/Cbfb-deleted MLL-AF9 cells. Similar to the effect of Runx1/Cbfb deletion, PAR-1 overexpression induced CDKN1A/p21 expression and attenuated proliferation in MLL-AF9 cells

our findings define a detrimental role of thrombin-activated PAR-1 in wound healing in mice with spinal cord injuries.

Matrix metalloproteinases (MMP) are effectors of hippocampal neuroplasticity in the adult central nervous system and that the MMP-1/protease-activated receptor-1 axis may play a role in neurogenesis following physiological and/or pathological stimuli.

Data indicate an involvement of protease-activated receptor-1 in the neuroinflammation mediated by Eomes(+) CD4(+) T cells.

MMP-1 promotes VEGFR2 expression and proliferation of endothelial cells through stimulation of PAR-1 and activation of NF-kappaB

PAR1 and PAR2 regulate endothelial NO synthase phosphorylation and activity through G(12/13) and G(q), delineating the signaling pathways by which the proteases act on protease-activated receptors to modulate endothelial functions.

F2R profil antigène

Antigen Summary

Coagulation factor II receptor is a 7-transmembrane receptor involved in the regulation of thrombotic response. Proteolytic cleavage leads to the activation of the receptor. F2R is a G-protein coupled receptor family member.